Purification and Some Properties of Chitinase from the Stomach of Japanese Eel, Anguilla japonica

Chitinase (EC 3.2.1.14) was purified from the stomach of Japanese eel, Anguilla japonica, by fractionations with ammonium sulfate, Sephadex G-100 gel filtration, and DEAE-cellulose, CM-cellulose, and hydroxylapatite column chromatography. The molecular weight of this enzyme was 50,000 by SDS-PAGE, a...

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Published inAgricultural and biological chemistry Vol. 54; no. 4; pp. 973 - 978
Main Authors Kono, Michiko, Matsui, Takashi, Shimizu, Chiaki, Koga, Daizo
Format Journal Article
LanguageEnglish
Published Taylor & Francis 01.04.1990
Subjects
Anguilla japonica
biochemical analysis
Brackish
characterization
chitinase
enzymes
Freshwater
Marine
purification
stomach
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Summary:Chitinase (EC 3.2.1.14) was purified from the stomach of Japanese eel, Anguilla japonica, by fractionations with ammonium sulfate, Sephadex G-100 gel filtration, and DEAE-cellulose, CM-cellulose, and hydroxylapatite column chromatography. The molecular weight of this enzyme was 50,000 by SDS-PAGE, and the optimum pH was 4.4. The activity was strongly inhibited by Hg 2+ and slightly activated by EDTA. The hydrolysis products of colloidal chitin by the enzyme were GlcNAc and GlcNAc 2 . When GlcNAc 3-6 was used as substrate, GlcNAc and GlcNAc 2 were recognized as final products with various ratios. GlcNAc 2 was not hydrolyzed by this chitinase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0002-1369
DOI:10.1080/00021369.1990.10870054